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Title: Rubisco: Active-site characterization and mechanistic implications

Abstract

Diverse chemical methods and comparative sequence analyses have identified Lys-166, Lys-329, and Glu-48 of Rubisco as active-site residues and have suggested that these residues participate in catalysis. These conclusions have been validated by site-directed mutagenesis; furthermore, hybridization of distinct site-directed mutant proteins demonstrates an intersubunit location of the active site in which side chains from each subunit are required. The ability of mutant proteins, devoid of overall carboxylase activity, to catalyze certain partial reactions suggests that Lys-166 is the base that enolizes ribulose-P/sub 2/ and that Lys-329 facilitates addition of gaseous substrate to the enediol. 39 refs., 6 figs., 2 tabs.

Authors:
Publication Date:
Research Org.:
Oak Ridge National Lab., TN (USA)
OSTI Identifier:
5999278
Report Number(s):
CONF-8906166-1
ON: DE89014066
DOE Contract Number:  
AC05-84OR21400
Resource Type:
Conference
Resource Relation:
Conference: NATO Advanced Study Institute summer school of enzymatic and model carboxylation and reduction reactions for carbon dioxide utilization, Bari, Italy, 17-28 Jun 1989; Other Information: Portions of this document are illegible in microfiche products
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; MOLECULAR STRUCTURE; DETECTION; PROTEINS; AMINO ACID SEQUENCE; BIOCHEMICAL REACTION KINETICS; CATALYSIS; HYBRIDIZATION; MUTAGENS; PROTEIN STRUCTURE; KINETICS; ORGANIC COMPOUNDS; REACTION KINETICS; 550200* - Biochemistry

Citation Formats

Hartman, F C. Rubisco: Active-site characterization and mechanistic implications. United States: N. p., 1989. Web.
Hartman, F C. Rubisco: Active-site characterization and mechanistic implications. United States.
Hartman, F C. Sun . "Rubisco: Active-site characterization and mechanistic implications". United States.
@article{osti_5999278,
title = {Rubisco: Active-site characterization and mechanistic implications},
author = {Hartman, F C},
abstractNote = {Diverse chemical methods and comparative sequence analyses have identified Lys-166, Lys-329, and Glu-48 of Rubisco as active-site residues and have suggested that these residues participate in catalysis. These conclusions have been validated by site-directed mutagenesis; furthermore, hybridization of distinct site-directed mutant proteins demonstrates an intersubunit location of the active site in which side chains from each subunit are required. The ability of mutant proteins, devoid of overall carboxylase activity, to catalyze certain partial reactions suggests that Lys-166 is the base that enolizes ribulose-P/sub 2/ and that Lys-329 facilitates addition of gaseous substrate to the enediol. 39 refs., 6 figs., 2 tabs.},
doi = {},
url = {https://www.osti.gov/biblio/5999278}, journal = {},
number = ,
volume = ,
place = {United States},
year = {1989},
month = {1}
}

Conference:
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